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ZN574_XENTR
ID   ZN574_XENTR             Reviewed;         857 AA.
AC   Q6GL52;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Zinc finger protein 574;
GN   Name=znf574;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in transcriptional regulation.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; BC074658; AAH74658.1; -; mRNA.
DR   RefSeq; NP_001004843.1; NM_001004843.1.
DR   RefSeq; XP_012821811.1; XM_012966357.2.
DR   AlphaFoldDB; Q6GL52; -.
DR   SMR; Q6GL52; -.
DR   STRING; 8364.ENSXETP00000057402; -.
DR   PaxDb; Q6GL52; -.
DR   DNASU; 448126; -.
DR   Ensembl; ENSXETT00000057402; ENSXETP00000057402; ENSXETG00000027536.
DR   GeneID; 448126; -.
DR   KEGG; xtr:448126; -.
DR   CTD; 64763; -.
DR   Xenbase; XB-GENE-1004140; znf574.
DR   eggNOG; KOG1721; Eukaryota.
DR   HOGENOM; CLU_002678_24_1_1; -.
DR   InParanoid; Q6GL52; -.
DR   OMA; EDCAMEL; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; Q6GL52; -.
DR   TreeFam; TF350791; -.
DR   Proteomes; UP000008143; Chromosome 7.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000027536; Expressed in blastula and 13 other tissues.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00096; zf-C2H2; 7.
DR   SMART; SM00355; ZnF_C2H2; 20.
DR   SUPFAM; SSF57667; SSF57667; 10.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 18.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 19.
PE   2: Evidence at transcript level;
KW   DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..857
FT                   /note="Zinc finger protein 574"
FT                   /id="PRO_0000274866"
FT   ZN_FING         15..37
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         58..80
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         99..121
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         206..228
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         297..319
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         324..346
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         352..374
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         380..401
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         428..451
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         457..479
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         485..507
FT                   /note="C2H2-type 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         513..535
FT                   /note="C2H2-type 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         541..563
FT                   /note="C2H2-type 13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         569..591
FT                   /note="C2H2-type 14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         597..619
FT                   /note="C2H2-type 15; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         628..651
FT                   /note="C2H2-type 16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         681..703
FT                   /note="C2H2-type 17"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         709..731
FT                   /note="C2H2-type 18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         737..759
FT                   /note="C2H2-type 19"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         765..787
FT                   /note="C2H2-type 20"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          648..678
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        648..665
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   857 AA;  97090 MW;  B9F27F36B7DC3618 CRC64;
     MTDSEETVLY VEHRYVCSEC GEEYPSLEEA LEHQQSHAAA LQEPQYQIVG VNSLENQYQC
     LECGLLLRTP EDLLAHQELH PTQNEIQKPK RPTRSEIHYE CPECKALFNS QDVWMAHRYT
     HMQVQDVSHS KIVLQTDDHV IEDGLQLMCA PAVPSEVHLV TGDPHFHVST PSSASVSHTQ
     VLVDLEHSYK KNEGAGEDCA MELLLYKCSE CTQLFQTPGE FLEHQGTHFS GQERISDTNS
     HLDQTPQLSL NGQEKEPIIN QGNTCTDYQA ENKELLVQPE GEQAEQDSWT VDREPVFSCG
     DCSETFQTTK DLEEHQISHQ NGPFSCPLCS KVFPTYPEVG EHLKSHRSES RYLCVDCGLA
     FVSEAVLLNH RRSHLANPLF TCECGLTFLN MTRFLYHRRV HSSKQPDTGA VEEKKTVNSI
     APSPAGNFHC DPCGKDFPLL SQFLRHQRFV HALERRHKCP TCGKHFKKGS HLRTHMLTHT
     GERPYSCTVC SKSFNSQANL LRHRLTHTGE KPYKCQLCGK AFSQSSTLQQ HQYVHGQAYL
     YKCNECGINF HRPYRLLLHQ YHHTGEYPYK CQDCGLSFLL KRLLEVHQLG HRGEEPHRCR
     ECGTNFPSVQ RLQDHRCSKA GDGGGEKLEC PICGKKVTSD AHLNTHVAAQ HSGNKRSNVS
     SGKGTPVLPR NKLKGGGGKN LECSDCHKTF STETSLQVHR RIHTGERPYP CPDCGKAFRQ
     STHLKDHRRL HTGEKPFKCD VCGKAFTIAV RLSEHKRIHT GERPHSCPDC GRAYRSFSNL
     WKHRKLHREQ QVQLQEPESQ PADLSSTVAI LETVETIPII ETVEIFPEGS TISVQDIQFE
     TLQVENIHLG NIQIGTL
 
 
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